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» Prediction of the Number of Residue Contacts in Proteins
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BMCBI
2008
176views more  BMCBI 2008»
13 years 7 months ago
H2r: Identification of evolutionary important residues by means of an entropy based analysis of multiple sequence alignments
Background: A multiple sequence alignment (MSA) generated for a protein can be used to characterise residues by means of a statistical analysis of single columns. In addition to t...
Rainer Merkl, Matthias Zwick
CPM
2004
Springer
168views Combinatorics» more  CPM 2004»
14 years 26 days ago
The Protein Sequence Design Problem in Canonical Model on 2D and 3D Lattices
In this paper we investigate the protein sequence design (PSD) problem (also known as the inverse protein folding problem) under the Canonical model 4 on 2D and 3D lattices [12, 25...
Piotr Berman, Bhaskar DasGupta, Dhruv Mubayi, Robe...
BIBM
2007
IEEE
104views Bioinformatics» more  BIBM 2007»
13 years 11 months ago
A Protocol to Detect Local Affinities Involved in Proteins Distant Interactions
The tridimensional structure of a protein is constrained or stabilized by some local interactions between distant residues of the protein, such as disulfide bonds, electrostatic i...
Christophe Nicolas Magnan, Cécile Capponi, ...
BMCBI
2007
117views more  BMCBI 2007»
13 years 7 months ago
Supervised multivariate analysis of sequence groups to identify specificity determining residues
Background: Proteins that evolve from a common ancestor can change functionality over time, and it is important to be able identify residues that cause this change. In this paper ...
Iain M. Wallace, Desmond G. Higgins
BMCBI
2008
135views more  BMCBI 2008»
13 years 7 months ago
Functional site prediction selects correct protein models
Background: The prediction of protein structure can be facilitated by the use of constraints based on a knowledge of functional sites. Without this information it is still possibl...
Vijayalakshmi Chelliah, William R. Taylor